Literature summary for 2.7.1.183 extracted from

Nagae, M.; Mishra, S.K.; Neyazaki, M.; Oi, R.; Ikeda, A.; Matsugaki, N.; Akashi, S.; Manya, H.; Mizuno, M.; Yagi, H.; Kato, K.; Senda, T.; Endo, T.; Nogi, T.; Yamaguchi, Y.
3D structural analysis of protein O-mannosyl kinase, POMK, a causative gene product of dystroglycanopathy (2017), Genes Cells, 22, 348-359 .

Search for more literature for 2.7.1.183

Cloned(Commentary)

Cloned (Comment)	Organism
gene pomk, recombinant expression of th POMK catalytic domain in HEK-293 cells as a homogeneous glycoprotein with Man5GlcNAc2 structure, the deconvoluted ESI-MS spectrum showed three peaks, which correspond to singly N-glycosylated, doubly N-glycosylated and triply N-glycosylated proteins: N66 and N164 are partially glycosylated, whereas N219 is fully glycosylated	Mus musculus

Crystallization (Commentary)

Crystallization (Comment)	Organism
POMK catalytic domain mutant N66Q/N164Q, X-ray diffraction structure determination and analysis at 2.5 A resolution	Mus musculus

Protein Variants

Protein Variants	Comment	Organism
additional information	disease mutation mapping onto POMK structure	Mus musculus
N66Q/N164Q	site-directed mutagenesis, N66Q is located in the N-terminal loop region and close to a symmetry-related molecule, while N164Q is located at the alpha2-alpha3 loop	Mus musculus

KM Value [mM]

KM Value [mM]	KM Value Maximum [mM]	Substrate	Comment	Organism	Structure
0.0041	-	ATP	pH and temperature not specified in the publication, recombinant murine POMK catalytic domain	Mus musculus

Metals/Ions

Metals/Ions	Comment	Organism	Structure
Mg2+	required, the enzyme is fully active in the presence of manganese or magnesium ions	Mus musculus
Mn2+	required, the enzyme is fully active in the presence of manganese or magnesium ions	Mus musculus

Natural Substrates/ Products (Substrates)

Natural Substrates	Organism	Comment (Nat. Sub.)	Natural Products	Comment (Nat. Pro.)	Rev.	Reac.
ATP + 3-O-[N-acetyl-beta-D-galactosaminyl-(1->3)-N-acetyl-beta-D-glucosaminyl-(1->4)-alpha-D-mannosyl]-L-seryl-[protein]	Mus musculus	-	ADP + 3-O-[N-acetyl-beta-D-galactosaminyl-(1->3)-N-acetyl-beta-D-glucosaminyl-(1->4)-6-O-phosphono-alpha-D-mannosyl]-L-seryl-[protein]	-	?
ATP + 3-O-[N-acetyl-beta-D-galactosaminyl-(1->3)-N-acetyl-beta-D-glucosaminyl-(1->4)-alpha-D-mannosyl]-L-threonyl-[protein]	Mus musculus	-	ADP + 3-O-[N-acetyl-beta-D-galactosaminyl-(1->3)-N-acetyl-beta-D-glucosaminyl-(1->4)-6-O-phosphono-alpha-D-mannosyl]-L-threonyl-[protein]	-	?

Organism

Organism	UniProt	Comment	Textmining
Mus musculus	Q3TUA9	-	-

Posttranslational Modification

Posttranslational Modification	Comment	Organism
glycoprotein	murine POMK catalytic domain (residue 45-349) possesses three potential N-glycosylation sites, N66, N164 and N219, which are not conserved among species	Mus musculus

Substrates and Products (Substrate)

Substrates	Comment Substrates	Organism	Products	Comment (Products)	Rev.	Reac.
ATP + 3-O-[N-acetyl-beta-D-galactosaminyl-(1->3)-N-acetyl-beta-D-glucosaminyl-(1->4)-alpha-D-mannosyl]-L-seryl-[protein]	-	Mus musculus	ADP + 3-O-[N-acetyl-beta-D-galactosaminyl-(1->3)-N-acetyl-beta-D-glucosaminyl-(1->4)-6-O-phosphono-alpha-D-mannosyl]-L-seryl-[protein]	-	?
ATP + 3-O-[N-acetyl-beta-D-galactosaminyl-(1->3)-N-acetyl-beta-D-glucosaminyl-(1->4)-alpha-D-mannosyl]-L-threonyl-[protein]	-	Mus musculus	ADP + 3-O-[N-acetyl-beta-D-galactosaminyl-(1->3)-N-acetyl-beta-D-glucosaminyl-(1->4)-6-O-phosphono-alpha-D-mannosyl]-L-threonyl-[protein]	-	?

Subunits

Subunits	Comment	Organism
More	the POMK catalytic domain takes a typical protein kinase fold consisting of N- and C-lobes. The N-lobe goes from C54 to P152 and comprises five beta-strands arranged in an antiparallel beta-sheet with two alpha-helices (alpha1-2), whereas C-lobe is from L153 to L337 and is composed of nine alpha-helices (alpha3-11) with a beta-hairpin (beta6-7)	Mus musculus

Synonyms

Synonyms	Comment	Organism
POMK	-	Mus musculus
protein O-mannosyl kinase	-	Mus musculus
SGK196	-	Mus musculus

Cofactor

Cofactor	Comment	Organism	Structure
ATP	-	Mus musculus

General Information

General Information	Comment	Organism
evolution	POMK and FAM20 family proteins do not share a common ancestor or POMK evolutionarily isolated from a common ancestor at a very early time	Mus musculus
malfunction	several missense mutations of the POMK catalytic domain are known to cause a severe congenital muscular dystrophy, Walker-Warburg syndrome. Aberrant O-mannosylation of alpha-DG leads to severe congenital muscular dystrophies due to detachment of ECM proteins from the basal membrane. Disease mutation mapping onto POMK structure	Mus musculus
metabolism	orchestration of the multiple enzymes engaged in O-mannose glycan synthesis provides a matriglycan on alpha-dystroglycan (alpha-DG) which attracts extracellular matrix (ECM) proteins such as laminin. phosphorylation at C6-position of O-mannose catalyzed by protein O-mannosyl kinase (POMK) is a crucial step in the biosynthetic pathway of O-mannose glycan	Mus musculus
additional information	the POMK catalytic domain shows a typical protein kinase fold consisting of N- and C-lobes. Mannose residue binds to POMK mainly via the hydroxyl group at C2-position, differentiating from other monosaccharide residues. Intriguingly, the two amino acid residues K92 and D228, interacting with the triphosphate group of ATP, are donated from atypical positions in the primary structure. Protein O-mannosyl kinase (POMK) catalytic domain shows a typical kinase fold, recombinant murne POMK catalytic domain structure, overview. Docking model of POMK in complex with AMP-PNP and the trisaccharide unit (GalNAcbeta1-3GlcNAcbeta1-4Man) and molecular dynamics simulations	Mus musculus
physiological function	phosphorylation at C6-position of O-mannose catalyzed by protein O-mannosyl kinase (POMK) is a crucial step in the biosynthetic pathway of O-mannose glycan	Mus musculus

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Release 2023.1 (January 2023)